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- W2182768186 abstract "A 3.7-kb DNAregionencoding partoftheRhodospirilum rubrum CO oxidation (coo) systemwas identified byusing oligonucleotide probes. Sequence analysis ofthecloned region indicated fourcomplete orpartial open reading frames (ORFs) withacceptable codon usage.Thecomplete ORFs,the573-bp cooFandthe1,920-bp cooS, encode an Fe/Sprotein andtheNi-containing carbonmonoxide dehydrogenase (CODH),respectively. Thefour4-cysteine motifs encoded bycooFare typical ofa class ofproteins associated withother oxidoreductases, including formate dehydrogenase, nitrate reductase, dimethyl sulfoxide reductase, and hydrogenase activities. TheR.rubrum CODHis67%similar tothePsubunit oftheClosirhiium theroacetcwm CODH and47%similar tothea subunit oftheMethanoduix soehngenii CODH;an alignment ofthese three peptides showsrelativel limited overallconservation. Kanamycin cassette insertions intocooFandcooS resulted inR.rubrnmstrains devoid ofCO-dependent H2production withlittle (cooF::kan) orno (cooS:kan) methyl viologen-linked CODHactivity invitro, butdidnotdramatically alter their photoheterotrophic growth onmalate inthepresenceofCO.Upstream ofcooFisa567-bp partial ORF,designated cooH,that we ascribe totheCO-induced hydrogenase, based on sequencesimilarity withother hydrogenases andtheelimination of CO-dependent H2 production uponintroduction ofacassette into this region. Frommutantcharacterizations, we posit that cooHandcooFS arenotcotranscribed. Thesecond partial ORFstarts 67bpdownstream ofcooS andwouldbecapable ofencoding 35aminoacids with anATP-binding site motif. Carbon monoxide oxidation isaproperty ofnumerous bacterial genera withdiverse physiological characteristics. Thecarbon monoxide dehydrogenases (CODHs) ofaerobic organisms are02-stable three-subunit hydroxylases, often COinducible, that catalyze theoxidation ofCOtoCO2(38, 61). Theenzymes generally havehighaffinity forCO and couple its oxidation invitro withthereduction ofacceptors suchasmethylene blue; mostdonotreduce low-potential acceptors. Thepurified enzymescontain amolybdenum cofactor plusFeandperhaps Se,Zn,andCu(38). The structural genesfromPseudomonas thermocarboxydovorans havebeencloned (5). Inanaerobic organisms, including acetogens, dissimilatorysulfate reducers, andmethanogens, theCODHsare constitutively synthesized metalloproteins, usually 02labile, thatcatalyze theinterconversion ofsingle-carbon moieties withacetyl coenzyme A (acetyl-CoA); thereadily assayed oxidation ofCO toCO2(coupled withthereduction of low-potential electron acceptors) isbutonecatalytic function. Theinterconversion isafundamental anaerobic metabolic process, andthephysiology andbiochemistry ofthese bacteria havebeenthesubjects ofseveral reviews (29, 33, 43,54,62). Thepurified 190-kDa Methanothrix soehngenii protein contains 2Niplus18Featomsper(a13)2 tetramer, thenative formofthis enzyme(28). TheClostridium ther" @default.
- W2182768186 created "2016-06-24" @default.
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- W2182768186 date "1992-01-01" @default.
- W2182768186 modified "2023-09-27" @default.
- W2182768186 title "Genetic andPhysiological Characterization ofthe Rhodospinillum rubrumCarbonMonoxide Dehydrogenase System" @default.
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